ID F9ZR64_ACICS Unreviewed; 865 AA.
AC F9ZR64;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Atc_2152 {ECO:0000313|EMBL:AEK58800.1};
OS Acidithiobacillus caldus (strain SM-1).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK58800.1, ECO:0000313|Proteomes:UP000006135};
RN [1] {ECO:0000313|EMBL:AEK58800.1, ECO:0000313|Proteomes:UP000006135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK58800.1,
RC ECO:0000313|Proteomes:UP000006135};
RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT "Unraveling the Acidithiobacillus caldus complete genome and its central
RT metabolisms for carbon assimilation.";
RL J. Genet. Genomics 38:243-252(2011).
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP002573; AEK58800.1; -; Genomic_DNA.
DR RefSeq; WP_004873140.1; NC_015850.1.
DR AlphaFoldDB; F9ZR64; -.
DR STRING; 990288.Atc_2152; -.
DR GeneID; 69614543; -.
DR KEGG; acu:Atc_2152; -.
DR HOGENOM; CLU_005070_4_2_6; -.
DR OrthoDB; 5287200at2; -.
DR Proteomes; UP000006135; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000006135};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 405..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 96587 MW; DDB01C1CE8C38989 CRC64;
MRVDKLTTKF QQALQEAQSL ALARDHQQME PVHLLLAFLD QDGGIARPLL AKAGVRVDAL
RNALGRALES LPKVEGVPGE VQMGRDLGNL LNLADKIAQK RGDSYISTEH FLLALLEDRG
EAGRLFKEAG ASSKDLEQAV QELHGGEKIN DPNAEEQRQA LEKYTLDYTE RAAQGKLDPV
IGRDDEIRRT IQVLLRRSKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE SLRGKRLLGL
DLGALIAGAK FRGEFEERLK ALLNDLAKAE GKIILFIDEI HTLVGAGKAD GAMDAGNMLK
PALARGELHC IGATTLDEYR KYIEKDAALE RRFQRVLVDE PSVEDTIAIL RGLKERYEAH
HGVRITDPAL VAAAQLSHRY ISDRNLPDKA IDLVDEAASR IKMEIDSKPE ELDELERRLI
QLNIEKVALA KEKDEASRKR LENLESQIAE LQRKYQELEE IWKSEKLAIE GTSQIQKELD
RLRVELDNAR RANDLERMAQ IQYGQIPALE AKLREAEKQE ADGQRKAPTL LRTEVTEEEI
AEVISRWTGI PVSKMLEGEK EKLLKMEERL RARVVGQDEA VTAVANAIRR SRAGLADPRR
PIGSFLFLGP TGVGKTELTK ALAEFLFDSE DHMVRIDMSE FMEKHSVARL IGAPPGYVGY
EEGGYLTEAV RRKPYSVILL DEVEKAHPEV FNILLQVLDD GRLTDGQGRT VDFRNTVIVM
TSNLGSDRIQ EYGRLGDVEG MRGAVMEVVQ GHFRPEFLNR IDELVIFQPL SRQQLRAIAE
IQMGSLRARL RERDLDIVLS DAAVNLLAET GFDPVYGARP LKRVIQREIE NPLAQRLLRG
EFAPGQVIHV DAQGGQFVFG PSALH
//
